1Y5X | pdb_00001y5x

tRNA-guanine Transglycosylase (TGT) in complex with 6-Amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1y5xa_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	tRNA-guanine transglycosylase	tRNA-guanine transglycosylase	Queosine tRNA-guanine transglycosylase	(Zymomonas mobilis ) [TaxId: 542 ],	SCOPe (2.08)
B [auth D]	d1y5xd_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	tRNA-guanine transglycosylase	tRNA-guanine transglycosylase	Queosine tRNA-guanine transglycosylase	(Zymomonas mobilis ) [TaxId: 542 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	tRNA-guanine transglycosylase	8040041	3000635	SCOP2B (2022-06-29)
B [auth D]	SCOP2B Superfamily	tRNA-guanine transglycosylase	8040041	3000635	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	TGT	e1y5xA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TGT	ECOD (1.6)
B [auth D]	TGT	e1y5xD1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TGT	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.105	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Queuine tRNA-ribosyltransferase-like	CATH (4.3.0)
B [auth D]	3.20.20.105	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Queuine tRNA-ribosyltransferase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth D]	PF01702	Queuine tRNA-ribosyltransferase (TGT)	Queuine tRNA-ribosyltransferase	This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with que ...	This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyses the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position [1,2]. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth D]	Queuine tRNA-ribosyltransferase	pentosyltransferase activity glycosyltransferase activity catalytic activity, acting on RNA tRNA-guanosine(34) queuine transglycosylase activity catalytic activity, acting on a nucleic acid catalytic activity, acting on a tRNA transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate derivative biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process carbohydrate derivative metabolic process primary metabolic process ribonucleoside biosynthetic process nucleoside biosynthetic process nucleobase-containing compound biosynthetic process queuosine metabolic process nucleoside metabolic process nucleobase-containing small molecule biosynthetic process nucleobase-containing compound metabolic process queuosine biosynthetic process biosynthetic process carbohydrate derivative biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process carbohydrate derivative metabolic process primary metabolic process ribonucleoside biosynthetic process nucleoside biosynthetic process nucleobase-containing compound biosynthetic process queuosine metabolic process nucleoside metabolic process nucleobase-containing small molecule biosynthetic process nucleobase-containing compound metabolic process queuosine biosynthetic process biosynthetic process nucleobase-containing small molecule metabolic process small molecule metabolic process metabolic process cellular process ribonucleoside metabolic process tRNA modification RNA metabolic process tRNA-guanine transglycosylation gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process RNA biosynthetic process nucleic acid biosynthetic process RNA modification tRNA processing macromolecule modification macromolecule metabolic process RNA processing tRNA wobble guanine modification tRNA wobble base modification	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth D]	IPR036511	Queuine tRNA-ribosyltransferase-like	Homologous Superfamily
A, B [auth D]	IPR004803	tRNA-guanine transglycosylase	Family
A, B [auth D]	IPR050076	Archaeosine Synthase Type 1/Queuine TRNA-Ribosyltransferase	Family
A, B [auth D]	IPR002616	tRNA-guanine(15) transglycosylase-like	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.